TRPA_CAUVN
ID TRPA_CAUVN Reviewed; 275 AA.
AC B8H661;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; OrderedLocusNames=CCNA_03657;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
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DR EMBL; CP001340; ACL97122.1; -; Genomic_DNA.
DR RefSeq; WP_010921372.1; NC_011916.1.
DR RefSeq; YP_002519030.1; NC_011916.1.
DR AlphaFoldDB; B8H661; -.
DR SMR; B8H661; -.
DR PRIDE; B8H661; -.
DR EnsemblBacteria; ACL97122; ACL97122; CCNA_03657.
DR GeneID; 7329748; -.
DR KEGG; ccs:CCNA_03657; -.
DR PATRIC; fig|565050.3.peg.3566; -.
DR HOGENOM; CLU_016734_0_0_5; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 912786at2; -.
DR PhylomeDB; B8H661; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..275
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_1000198704"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 275 AA; 28520 MW; C275DA90C80B271F CRC64;
MTKDRIDRRF AALKAENRAG FVTYVMAGDP DAATTLSVLK GLPAAGADLI ELGFPFSDPM
AEGPTIQRAA QRGLKSGMTL QGTLDLVAAF REGDQDTPII LMGYLNPVLN KGFETFAALA
AKAGVDGLII VDCPPEEADP LSDALEAEGI ALIRLAAPTT DDARLPMVVR RTSGFVYYVS
VAGVTGVKSA DAADVAPAVE RLRKASGLPV AVGFGIRTPD QAAAVAKVAD AAVVGSALVD
EIESAAQLNE NVTEKVLLKA SELAKAVRSA RVGTK
